Intrinsically disordered proteins lack a hydrophobic core, and have high densities of charged amino acid residues such as Lys, Arg, and Glu. Pro residues are also prominent, as they tend to disrupt ordered structures.

TLS Online TPP Program

#Id: 8269

#Unit 1. Molecules and their Interaction Relevant to Biology

Nitrogenous Base pairs & aromatic amino acids stack together through pi, pi-electronic interactions. These stacking interactions are best example of VWI.

TLS Online TPP Program

#Id: 8270

#Unit 1. Molecules and their Interaction Relevant to Biology

TLS Online TPP Program

#Id: 8271

#Unit 1. Molecules and their Interaction Relevant to Biology

Misplaced Dispersion forces are responsible for

1. Sickle-Cell Anemia

2. Alzheimer's disease

3. CFTR

4. Huntington disease

TLS Online TPP Program

#Id: 8272

#Unit 1. Molecules and their Interaction Relevant to Biology

A hydrogen bond is an intermolecular force (IMF) that forms a special type of dipole-dipole attraction when a hydrogen atom bonded to a strongly electronegative atom exists in the vicinity of another electronegative atom with a lone pair of electrons.

TLS Online TPP Program

#Id: 8273

#Unit 1. Molecules and their Interaction Relevant to Biology

Hydrogen bonds are generally stronger than ordinary dipole-dipole and dispersion forces, but weaker than true covalent and ionic bonds.

TLS Online TPP Program

#Id: 8274

#Unit 1. Molecules and their Interaction Relevant to Biology

Two Requirements for Hydrogen Bonding:

First molecules has hydrogen attached to a highly electronegative atom (N, O, F) called as (hydrogen bond donor)

Second molecule has a lone pair of electrons on a small highly electronegative atom (N, O, F) called as (hydrogen bond acceptor)